Sandbox GGC1
From Proteopedia
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== Chymotrypsin == | == Chymotrypsin == | ||
<StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | <StructureSection load='1T8L' size='340' side='right' caption='Bovine chymotrypsin complexes with P1 BPTI variants' scene='75/752263/Intro/1'> | ||
| - | Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. | + | Chymotrypsin is a protease, which is an enzyme that catalyzes the cleavage of amino acids at the carboxyl side. The active site is referred to as the P1 position. The S1 binding pocket is responsible for stabilization of the P1 substrate prior to cleavage. |
This is a default text for your page '''Chymotrypsin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Chymotrypsin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
Revision as of 15:40, 10 April 2017
Chymotrypsin
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References
- ↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088
- ↑ Czapinska H, Helland R, Smalas AO, Otlewski J. Crystal structures of five bovine chymotrypsin complexes with P1 BPTI variants. J Mol Biol. 2004 Dec 3;344(4):1005-20. PMID:15544809 doi:10.1016/j.jmb.2004.09.088
